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Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates

Mörgelin, Matthias LU ; Paulsson, Mats; Heinegård, Dick LU ; Aebi, Ueli and Engel, Jürgen (1995) In Biochemical Journal 307(Pt 2). p.595-601
Abstract
Aggregates of proteoglycans from the Swarm rat chondrosarcoma reassembled in vitro have been studied by rotary-shadowing electron microscopy, and shown to be similar to native structures that have never been dissociated [Morgelin, Engel, Heinegard and Paulsson (1992) J. Biol. Chem. 267, 14275-14284]. A hyaluronate with defined chain length (HAshort) has now been prepared by autoclaving high-Mr hyaluronate and fractionation to a narrow size distribution by gel filtration. Proteoglycan monomers, core protein, hyaluronate-binding region and link protein were combined with HAshort. Free chains of HAshort and reconstituted complexes with proteoglycan, link protein and aggrecan fragments were examined by electron microscopy after rotary... (More)
Aggregates of proteoglycans from the Swarm rat chondrosarcoma reassembled in vitro have been studied by rotary-shadowing electron microscopy, and shown to be similar to native structures that have never been dissociated [Morgelin, Engel, Heinegard and Paulsson (1992) J. Biol. Chem. 267, 14275-14284]. A hyaluronate with defined chain length (HAshort) has now been prepared by autoclaving high-Mr hyaluronate and fractionation to a narrow size distribution by gel filtration. Proteoglycan monomers, core protein, hyaluronate-binding region and link protein were combined with HAshort. Free chains of HAshort and reconstituted complexes with proteoglycan, link protein and aggrecan fragments were examined by electron microscopy after rotary shadowing. Length measurements showed that the hyaluronate was condensed to about half of its original length on binding intact aggrecan monomers, any aggrecan fragment or link protein alone. This strongly implies that hyaluronate adopts a defined spatial arrangement within the central filament of the aggregate, probably different from its secondary structure in solution. No differences in length were observed between link-free and link-stabilized aggregates. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Biochemical Journal
volume
307
issue
Pt 2
pages
595 - 601
publisher
Portland Press Limited
external identifiers
  • pmid:7733901
  • scopus:0028933622
ISSN
0264-6021
language
English
LU publication?
yes
id
014682f6-a17d-4acd-a487-c764ca5f61d3 (old id 1109427)
alternative location
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1136689
date added to LUP
2008-07-28 14:31:18
date last changed
2017-01-01 06:42:30
@article{014682f6-a17d-4acd-a487-c764ca5f61d3,
  abstract     = {Aggregates of proteoglycans from the Swarm rat chondrosarcoma reassembled in vitro have been studied by rotary-shadowing electron microscopy, and shown to be similar to native structures that have never been dissociated [Morgelin, Engel, Heinegard and Paulsson (1992) J. Biol. Chem. 267, 14275-14284]. A hyaluronate with defined chain length (HAshort) has now been prepared by autoclaving high-Mr hyaluronate and fractionation to a narrow size distribution by gel filtration. Proteoglycan monomers, core protein, hyaluronate-binding region and link protein were combined with HAshort. Free chains of HAshort and reconstituted complexes with proteoglycan, link protein and aggrecan fragments were examined by electron microscopy after rotary shadowing. Length measurements showed that the hyaluronate was condensed to about half of its original length on binding intact aggrecan monomers, any aggrecan fragment or link protein alone. This strongly implies that hyaluronate adopts a defined spatial arrangement within the central filament of the aggregate, probably different from its secondary structure in solution. No differences in length were observed between link-free and link-stabilized aggregates.},
  author       = {Mörgelin, Matthias and Paulsson, Mats and Heinegård, Dick and Aebi, Ueli and Engel, Jürgen},
  issn         = {0264-6021},
  language     = {eng},
  number       = {Pt 2},
  pages        = {595--601},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates},
  volume       = {307},
  year         = {1995},
}